| 纯度 | >90%SDS-PAGE. |
| 种属 | Mouse |
| 靶点 | Mup11 |
| Uniprot No | P04938 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 32-181 aa |
| 氨基酸序列 | EKINGEWHTIILASDKREKIEDNGNFRLFLEQIHVLENSLVLKFHTVRDEECSELSMVADKTEKAGEYSVTYDGFNTFTIPKTDYDNFLMAHLINEKDGETFQLMGLYGREPDLSSDIKERFAQLCEEHGILRENIIDLSNANRCLQARE |
| 预测分子量 | 19.6 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于Mup11重组蛋白的3篇模拟参考文献(内容基于学术文献常见主题整理，非真实文献)：
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1. **文献名称**：*Expression and Purification of Recombinant Mup11 in Escherichia coli*
**作者**：Smith A., et al.
**摘要**：本研究报道了通过大肠杆菌表达系统高效表达和纯化Mup11重组蛋白的优化方法，包括密码子优化、诱导条件筛选及亲和层析纯化策略，为后续功能研究提供高纯度蛋白。
2. **文献名称**：*Structural Characterization of Mup11 Reveals Pheromone-Binding Specificity*
**作者**：Zhang L., et al.
**摘要**：通过X射线晶体学解析Mup11重组蛋白的三维结构，发现其独特的疏水结合口袋可特异性识别小鼠信息素分子，揭示了其在化学通讯中的潜在作用机制。
3. **文献名称**：*Functional Analysis of Recombinant Mup11 in Olfactory Signaling Pathways*
**作者**：Johnson R., et al.
**摘要**：利用体外结合实验和细胞模型证明，重组Mup11蛋白可增强嗅觉受体神经元对特定信息素的响应，提示其可能在哺乳动物信息素传递中作为载体蛋白发挥作用。
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注：以上文献及摘要均为模拟生成，实际研究中请通过PubMed、Web of Science等平台检索真实文献。
**Background of Mup11 Recombinant Protein**
Mup11 (Major urinary protein 11) belongs to the lipocalin family of proteins, which are small extracellular molecules known for binding and transporting hydrophobic ligands. Primarily studied in rodents, MUPs are abundant in urine and play roles in chemical communication, pheromone signaling, and metabolic regulation. Mup11. specifically, is expressed in the liver and secreted into the bloodstream before being filtered into urine. Its structure features a conserved β-barrel fold that facilitates ligand binding, such as fatty acids or pheromones, enabling it to act as a signaling mediator in social and reproductive behaviors.
The production of recombinant Mup11 leverages genetic engineering to express the protein in heterologous systems (e.g., *E. coli* or yeast), bypassing the need for native tissue extraction. This approach ensures high purity, scalability, and customization (e.g., tagging for detection or affinity purification). Recombinant Mup11 retains its ligand-binding properties, making it valuable for studying protein-ligand interactions, cellular uptake mechanisms, and its role in metabolic pathways.
Research on Mup11 has expanded beyond its physiological context. It serves as a model for understanding lipocalin function and has potential applications in biotechnology, such as drug delivery systems due to its ligand-carrying capacity. Additionally, studies link MUPs to metabolic diseases and cancer, positioning recombinant Mup11 as a tool for exploring these associations. Despite progress, questions remain about its full ligand spectrum, tissue-specific roles, and evolutionary conservation in non-rodent species.
In summary, recombinant Mup11 bridges molecular biology and translational research, offering insights into both fundamental protein mechanisms and therapeutic opportunities.
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